Abstract
The high-producing strain С3029/pGro7/pERDerp3 for the house dust mite allergen Der p 3 from Dermatophagoides pteronyssinus, expressing the recombinant protein in Escherichia coli in the soluble form, was constructed. A procedure was developed for the purification of the recombinant allergen. Crystals of the recombinant protein Der p 3 suitable for X-ray diffraction analysis were grown by the vapor-diffusion method. The X-ray diffraction data set was collected to 2.25 Å resolution at the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K. The crystals belong to sp. gr. С121 and contain two enzyme molecules per asymmetric unit.
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